The folding of hen lysozyme involves partially structured intermediates and multiple pathways

Nature. 1992 Jul 23;358(6384):302-7. doi: 10.1038/358302a0.


Analysis of the folding of hen lysozyme shows that the protein does not become organized in a single cooperative event but that different parts of the structure become stabilized with very different kinetics. In particular, in most molecules the alpha-helical domain folds faster than the beta-sheet domain. Furthermore, different populations of molecules fold by kinetically distinct pathways. Thus, folding is not a simple sequential assembly process but involves parallel alternative pathways, some of which may involve substantial reorganization steps.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chickens
  • Circular Dichroism
  • Female
  • Hydrogen-Ion Concentration
  • Kinetics
  • Models, Molecular
  • Muramidase / chemistry*
  • Muramidase / metabolism
  • Protein Conformation
  • Time Factors


  • Muramidase